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Volumn 395, Issue 2, 2009, Pages 298-311

Nipah virus entry can occur by macropinocytosis

Author keywords

Antivirals; Entry; Macropinocytosis; Nipah virus

Indexed keywords

2 MORPHOLINO 8 PHENYLCHROMONE; 5 (N ETHYL N ISOPROPYL)AMILORIDE; BLEBBISTATIN; CHLOROQUINE; EPHRIN B2; GENISTEIN; LATRUNCULIN A; PHENYLALANINE; TYROSINE; WORTMANNIN;

EID: 70450223511     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2009.09.016     Document Type: Article
Times cited : (55)

References (50)
  • 1
    • 17844406602 scopus 로고    scopus 로고
    • Bacterial cytotoxins: targeting eukaryotic switches
    • Aktories K., and Barbieri J.T. Bacterial cytotoxins: targeting eukaryotic switches. Nat. Rev. Microbiol. 3 5 (2005) 397-410
    • (2005) Nat. Rev. Microbiol. , vol.3 , Issue.5 , pp. 397-410
    • Aktories, K.1    Barbieri, J.T.2
  • 5
    • 33846844906 scopus 로고    scopus 로고
    • Newcastle disease virus may enter cells by caveolae-mediated endocytosis
    • Cantin C., Holguera J., Ferreira L., Villar E., and Munoz-Barroso I. Newcastle disease virus may enter cells by caveolae-mediated endocytosis. J. Gen. Virol. 88 Pt 2 (2007) 559-569
    • (2007) J. Gen. Virol. , vol.88 , Issue.PART 2 , pp. 559-569
    • Cantin, C.1    Holguera, J.2    Ferreira, L.3    Villar, E.4    Munoz-Barroso, I.5
  • 7
    • 0037018152 scopus 로고    scopus 로고
    • Identification of an adaptor-associated kinase, AAK1, as a regulator of clathrin-mediated endocytosis
    • Conner S.D., and Schmid S.L. Identification of an adaptor-associated kinase, AAK1, as a regulator of clathrin-mediated endocytosis. J. Cell Biol. 156 5 (2002) 921-929
    • (2002) J. Cell Biol. , vol.156 , Issue.5 , pp. 921-929
    • Conner, S.D.1    Schmid, S.L.2
  • 8
    • 0035855819 scopus 로고    scopus 로고
    • The SH2/SH3 adaptor Grb4 transduces B-ephrin reverse signals
    • Cowan C.A., and Henkemeyer M. The SH2/SH3 adaptor Grb4 transduces B-ephrin reverse signals. Nature 413 6852 (2001) 174-179
    • (2001) Nature , vol.413 , Issue.6852 , pp. 174-179
    • Cowan, C.A.1    Henkemeyer, M.2
  • 11
    • 43249094400 scopus 로고    scopus 로고
    • Role of endocytosis and cathepsin-mediated activation in Nipah virus entry
    • Diederich S., Thiel L., and Maisner A. Role of endocytosis and cathepsin-mediated activation in Nipah virus entry. Virology 375 2 (2008) 391-400
    • (2008) Virology , vol.375 , Issue.2 , pp. 391-400
    • Diederich, S.1    Thiel, L.2    Maisner, A.3
  • 12
    • 5644229850 scopus 로고    scopus 로고
    • Earp, L. J., Delos, S.E., Park, H.E., and White, J.M. (2004). The many mechanisms of viral membrane fusion proteins. In In : R.W. Compans, M.D. Cooper, T. Honjo, H. Kaprowski H, Melchers F, Oldstone MBA, Olnes S, Potter M, et al. (Eds), Curr. Top. Microbiol. Immunol. 285: Springer-Verlag, New-York, pp. 25-66. Springer-Verlag, New-York.
    • Earp, L. J., Delos, S.E., Park, H.E., and White, J.M. (2004). The many mechanisms of viral membrane fusion proteins. In "In : R.W. Compans, M.D. Cooper, T. Honjo, H. Kaprowski H, Melchers F, Oldstone MBA, Olnes S, Potter M, et al. (Eds), Curr. Top. Microbiol. Immunol. 285: Springer-Verlag, New-York", pp. 25-66. Springer-Verlag, New-York.
  • 15
    • 33746214691 scopus 로고    scopus 로고
    • Evidence of a potential receptor-binding site on the Nipah virus G protein (NiV-G): identification of globular head residues with a role in fusion promotion and their localization on an NiV-G structural model
    • Guillaume V., Aslan H., Ainouze M., Guerbois M., Wild T.F., Buckland R., and Langedijk J.P. Evidence of a potential receptor-binding site on the Nipah virus G protein (NiV-G): identification of globular head residues with a role in fusion promotion and their localization on an NiV-G structural model. J. Virol. 80 15 (2006) 7546-7554
    • (2006) J. Virol. , vol.80 , Issue.15 , pp. 7546-7554
    • Guillaume, V.1    Aslan, H.2    Ainouze, M.3    Guerbois, M.4    Wild, T.F.5    Buckland, R.6    Langedijk, J.P.7
  • 17
    • 0029851690 scopus 로고    scopus 로고
    • Bidirectional signalling through the EPH-family receptor Nuk and its transmembrane ligands
    • Holland S.J., Gale N.W., Mbamalu G., Yancopoulos G.D., Henkemeyer M., and Pawson T. Bidirectional signalling through the EPH-family receptor Nuk and its transmembrane ligands. Nature 383 6602 (1996) 722-725
    • (1996) Nature , vol.383 , Issue.6602 , pp. 722-725
    • Holland, S.J.1    Gale, N.W.2    Mbamalu, G.3    Yancopoulos, G.D.4    Henkemeyer, M.5    Pawson, T.6
  • 18
    • 0032487332 scopus 로고    scopus 로고
    • Mechanisms of enveloped virus entry into animal cells
    • Klasse P.J., Bron R., and Marsh M. Mechanisms of enveloped virus entry into animal cells. Adv. Drug Deliv. Rev. 34 1 (1998) 65-91
    • (1998) Adv. Drug Deliv. Rev. , vol.34 , Issue.1 , pp. 65-91
    • Klasse, P.J.1    Bron, R.2    Marsh, M.3
  • 19
    • 34447273317 scopus 로고    scopus 로고
    • Small interfering RNA profiling reveals key role of clathrin-mediated endocytosis and early endosome formation for infection by respiratory syncytial virus
    • Kolokoltsov A.A., Deniger D., Fleming E.H., Roberts Jr. N.J., Karpilow J.M., and Davey R.A. Small interfering RNA profiling reveals key role of clathrin-mediated endocytosis and early endosome formation for infection by respiratory syncytial virus. J. Virol. 81 14 (2007) 7786-7800
    • (2007) J. Virol. , vol.81 , Issue.14 , pp. 7786-7800
    • Kolokoltsov, A.A.1    Deniger, D.2    Fleming, E.H.3    Roberts Jr., N.J.4    Karpilow, J.M.5    Davey, R.A.6
  • 20
    • 0029807139 scopus 로고    scopus 로고
    • Lysosomal targeting of epidermal growth factor receptors via a kinase-dependent pathway is mediated by the receptor carboxyl-terminal residues 1022-1123
    • Kornilova E., Sorkina T., Beguinot L., and Sorkin A. Lysosomal targeting of epidermal growth factor receptors via a kinase-dependent pathway is mediated by the receptor carboxyl-terminal residues 1022-1123. J. Biol. Chem. 271 48 (1996) 30340-30346
    • (1996) J. Biol. Chem. , vol.271 , Issue.48 , pp. 30340-30346
    • Kornilova, E.1    Sorkina, T.2    Beguinot, L.3    Sorkin, A.4
  • 22
    • 0037128934 scopus 로고    scopus 로고
    • CD46 is phosphorylated at tyrosine 354 upon infection of epithelial cells by Neisseria gonorrhoeae
    • Lee S.W., Bonnah R.A., Higashi D.L., Atkinson J.P., Milgram S.L., and So M. CD46 is phosphorylated at tyrosine 354 upon infection of epithelial cells by Neisseria gonorrhoeae. J. Cell Biol. 156 6 (2002) 951-957
    • (2002) J. Cell Biol. , vol.156 , Issue.6 , pp. 951-957
    • Lee, S.W.1    Bonnah, R.A.2    Higashi, D.L.3    Atkinson, J.P.4    Milgram, S.L.5    So, M.6
  • 24
    • 0035815305 scopus 로고    scopus 로고
    • Ephrin-B reverse signaling is mediated by a novel PDZ-RGS protein and selectively inhibits G protein-coupled chemoattraction
    • Lu Q., Sun E.E., Klein R.S., and Flanagan J.G. Ephrin-B reverse signaling is mediated by a novel PDZ-RGS protein and selectively inhibits G protein-coupled chemoattraction. Cell 105 1 (2001) 69-79
    • (2001) Cell , vol.105 , Issue.1 , pp. 69-79
    • Lu, Q.1    Sun, E.E.2    Klein, R.S.3    Flanagan, J.G.4
  • 25
    • 32944473016 scopus 로고    scopus 로고
    • Virus entry: open sesame
    • Marsh M., and Helenius A. Virus entry: open sesame. Cell 124 4 (2006) 729-740
    • (2006) Cell , vol.124 , Issue.4 , pp. 729-740
    • Marsh, M.1    Helenius, A.2
  • 26
    • 0141839882 scopus 로고    scopus 로고
    • Rac-dependent trans-endocytosis of ephrinBs regulates Eph-ephrin contact repulsion
    • Marston D.J., Dickinson S., and Nobes C.D. Rac-dependent trans-endocytosis of ephrinBs regulates Eph-ephrin contact repulsion. Nat. Cell Biol. 5 (2003) 879-888
    • (2003) Nat. Cell Biol. , vol.5 , pp. 879-888
    • Marston, D.J.1    Dickinson, S.2    Nobes, C.D.3
  • 27
    • 12844264032 scopus 로고    scopus 로고
    • EphrinB2 expression in Karposi sarcoma is induced by human herpes type 8: phenotype switch from venous to arterial endothelium
    • Masood R., Guangbin X., Smith D.L., Scalia P., Still J.G., Tulpule A., and Gill P.S. EphrinB2 expression in Karposi sarcoma is induced by human herpes type 8: phenotype switch from venous to arterial endothelium. Blood 105 (2009) 1310-1318
    • (2009) Blood , vol.105 , pp. 1310-1318
    • Masood, R.1    Guangbin, X.2    Smith, D.L.3    Scalia, P.4    Still, J.G.5    Tulpule, A.6    Gill, P.S.7
  • 28
    • 4143051366 scopus 로고    scopus 로고
    • Measles virus (MV) hemagglutinin: evidence that attachment sites for MV receptors SLAM and CD46 overlap on the globular head
    • Masse N., Ainouze M., Neel B., Wild T.F., Buckland R., and Langedijk J.P. Measles virus (MV) hemagglutinin: evidence that attachment sites for MV receptors SLAM and CD46 overlap on the globular head. J. Virol. 78 17 (2004) 9051-9063
    • (2004) J. Virol. , vol.78 , Issue.17 , pp. 9051-9063
    • Masse, N.1    Ainouze, M.2    Neel, B.3    Wild, T.F.4    Buckland, R.5    Langedijk, J.P.6
  • 29
    • 42549153337 scopus 로고    scopus 로고
    • Vaccinia virus uses macropinocytosis and apoptotic mimicry to enter host cells
    • Mercer J., and Helenius A. Vaccinia virus uses macropinocytosis and apoptotic mimicry to enter host cells. Science 320 5875 (2008) 531-535
    • (2008) Science , vol.320 , Issue.5875 , pp. 531-535
    • Mercer, J.1    Helenius, A.2
  • 30
    • 65449120034 scopus 로고    scopus 로고
    • Virus entry by macropinocytosis
    • Mercer J., and Helenius A. Virus entry by macropinocytosis. Nature Cell Biol. 11 (2009) 510-520
    • (2009) Nature Cell Biol. , vol.11 , pp. 510-520
    • Mercer, J.1    Helenius, A.2
  • 33
    • 0027177368 scopus 로고
    • Measles virus haemagglutinin induces down-regulation of gp57/67, a molecule involved in virus binding
    • Naniche D., Wild T.F., Rabourdin-Combe C., and Gerlier D. Measles virus haemagglutinin induces down-regulation of gp57/67, a molecule involved in virus binding. J. Gen. Virol. 74 Pt 6 (1993) 1073-1079
    • (1993) J. Gen. Virol. , vol.74 , Issue.PART 6 , pp. 1073-1079
    • Naniche, D.1    Wild, T.F.2    Rabourdin-Combe, C.3    Gerlier, D.4
  • 36
    • 26444552119 scopus 로고    scopus 로고
    • Cathepsin L is involved in proteolytic processing of the Hendra virus fusion protein
    • Pager C.T., and Dutch R.E. Cathepsin L is involved in proteolytic processing of the Hendra virus fusion protein. J. Virol. 79 20 (2005) 12714-12720
    • (2005) J. Virol. , vol.79 , Issue.20 , pp. 12714-12720
    • Pager, C.T.1    Dutch, R.E.2
  • 37
    • 33644822934 scopus 로고    scopus 로고
    • A mature and fusogenic form of the Nipah virus fusion protein requires proteolytic processing by cathepsin L
    • Pager C.T., Craft W.W., Jr, Patch, J., and Dutch R.E. A mature and fusogenic form of the Nipah virus fusion protein requires proteolytic processing by cathepsin L. Virology 346 (2006) 251-257
    • (2006) Virology , vol.346 , pp. 251-257
    • Pager, C.T.1    Craft, W.W.2    Jr, Patch,, J.3    Dutch, R.E.4
  • 38
    • 33846533617 scopus 로고    scopus 로고
    • Quantitative analysis of Nipah virus proteins released as virus-like particles reveals central role for the matrix protein
    • Patch J.R., Crameri G., Wang L.F., Eaton B.T., and Broder C.C. Quantitative analysis of Nipah virus proteins released as virus-like particles reveals central role for the matrix protein. Virol. J. 4 (2007) 1
    • (2007) Virol. J. , vol.4 , pp. 1
    • Patch, J.R.1    Crameri, G.2    Wang, L.F.3    Eaton, B.T.4    Broder, C.C.5
  • 40
    • 0027278232 scopus 로고
    • Macropinosome maturation and fusion with tubular lysosomes in macrophages
    • Racoosin E.L., and Swanson J.A. Macropinosome maturation and fusion with tubular lysosomes in macrophages. J. Cell. Biol. 121 (1993) 1011-1020
    • (1993) J. Cell. Biol. , vol.121 , pp. 1011-1020
    • Racoosin, E.L.1    Swanson, J.A.2
  • 41
    • 33846813688 scopus 로고    scopus 로고
    • Inhibition of henipavirus infection by Nipah virus attachment glycoprotein occurs without cell-surface downregulation of ephrin-B2 or ephrin-B3
    • Sawatsky B., Grolla A., Kuzenko N., Weingartl H., and Czub M. Inhibition of henipavirus infection by Nipah virus attachment glycoprotein occurs without cell-surface downregulation of ephrin-B2 or ephrin-B3. J. Gen. Virol. 88 Pt 2 (2007) 582-591
    • (2007) J. Gen. Virol. , vol.88 , Issue.PART 2 , pp. 582-591
    • Sawatsky, B.1    Grolla, A.2    Kuzenko, N.3    Weingartl, H.4    Czub, M.5
  • 43
    • 2342471342 scopus 로고    scopus 로고
    • Single phosphorylation of Tyr304 in the cytoplasmic tail of ephrin B2 confers high-affinity and bifunctional binding to both the SH2 domain of Grb4 and the PDZ domain of the PDZ-RGS3 protein
    • Su Z., Xu P., and Ni F. Single phosphorylation of Tyr304 in the cytoplasmic tail of ephrin B2 confers high-affinity and bifunctional binding to both the SH2 domain of Grb4 and the PDZ domain of the PDZ-RGS3 protein. Eur. J. Biochem. 271 9 (2004) 1725-1736
    • (2004) Eur. J. Biochem. , vol.271 , Issue.9 , pp. 1725-1736
    • Su, Z.1    Xu, P.2    Ni, F.3
  • 44
    • 0036007494 scopus 로고    scopus 로고
    • The measles virus hemagglutinin downregulates the cellular receptor SLAM (CD150)
    • Tanaka K., Minagawa H., Xie M.F., and Yanagi Y. The measles virus hemagglutinin downregulates the cellular receptor SLAM (CD150). Arch. Virol. 147 1 (2002) 195-203
    • (2002) Arch. Virol. , vol.147 , Issue.1 , pp. 195-203
    • Tanaka, K.1    Minagawa, H.2    Xie, M.F.3    Yanagi, Y.4
  • 45
    • 62449212279 scopus 로고    scopus 로고
    • EphrinB2 expression critically influences Nipah virus infection independent of its cytoplasmic tail
    • Thiel L., Diederich S., Erbar S., Pfaff D., Augustin H.G., and Maisner A. EphrinB2 expression critically influences Nipah virus infection independent of its cytoplasmic tail. Virol. J. 5 (2008) 163
    • (2008) Virol. J. , vol.5 , pp. 163
    • Thiel, L.1    Diederich, S.2    Erbar, S.3    Pfaff, D.4    Augustin, H.G.5    Maisner, A.6
  • 46
    • 0024836461 scopus 로고
    • Distinct endocytotic pathways in epidermal growth factor-stimulated human carcinoma A431 cells
    • West M.A., Bretscher M.S., and Watts C. Distinct endocytotic pathways in epidermal growth factor-stimulated human carcinoma A431 cells. J. Cell Biol. 109 6 Pt 1 (1989) 2731-2739
    • (1989) J. Cell Biol. , vol.109 , Issue.6 PART 1 , pp. 2731-2739
    • West, M.A.1    Bretscher, M.S.2    Watts, C.3
  • 47
    • 0034644127 scopus 로고    scopus 로고
    • Rac is required for constitutive macropinocytosis by dendritic cells but does not control its downregulation
    • West M.A., Prescott A.R., Eskelinen E.L., Ridley A.J., and Watts C. Rac is required for constitutive macropinocytosis by dendritic cells but does not control its downregulation. Curr. Biol. 10 14 (2000) 839-848
    • (2000) Curr. Biol. , vol.10 , Issue.14 , pp. 839-848
    • West, M.A.1    Prescott, A.R.2    Eskelinen, E.L.3    Ridley, A.J.4    Watts, C.5
  • 48
    • 0141617343 scopus 로고    scopus 로고
    • How attraction turns to repulsion
    • Wilkinson D.G. How attraction turns to repulsion. Nat. Cell Biol. 5 10 (2003) 851-853
    • (2003) Nat. Cell Biol. , vol.5 , Issue.10 , pp. 851-853
    • Wilkinson, D.G.1
  • 50
    • 0141839883 scopus 로고    scopus 로고
    • EphB-ephrinB bi-directional endocytosis terminates adhesion allowing contact mediated repulsion
    • Zimmer M., Palmer A., Kohler J., and Klein R. EphB-ephrinB bi-directional endocytosis terminates adhesion allowing contact mediated repulsion. Nat. Cell Biol. 5 10 (2003) 869-878
    • (2003) Nat. Cell Biol. , vol.5 , Issue.10 , pp. 869-878
    • Zimmer, M.1    Palmer, A.2    Kohler, J.3    Klein, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.